1.1.1.202: 1,3-propanediol dehydrogenase
This is an abbreviated version!
For detailed information about 1,3-propanediol dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.202
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1.1.1.202
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pneumoniae
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klebsiella
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dehydratase
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synthesis
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fed-batch
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butyricum
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freundii
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citrobacter
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3-hydroxypropionic
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dissimilation
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1,2-propanediol
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pasteurianum
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eutropha
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biodiesel
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reuteri
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industry
- 1.1.1.202
- pneumoniae
- klebsiella
- dehydratase
- synthesis
-
fed-batch
- butyricum
- freundii
- citrobacter
-
3-hydroxypropionic
-
dissimilation
- 1,2-propanediol
- pasteurianum
-
eutropha
-
biodiesel
- reuteri
- industry
Reaction
Synonyms
(NADH)-linked 1,3-PD oxidoreductase, 1,3-PD dehydrogenase, 1,3-PD oxidoreductase, 1,3-PD-DH, 1,3-PD:NAD+ oxidoreductase, 1,3-PDDH, 1,3-Pdiol dehydrogenase, 1,3-propanediol dehydrogenase, 1,3-propanediol oxidoreductase, 1,3-propanediol-oxidoreductase, 1,3-propanediol-oxydoreductase, 1,3-propanediol:NAD oxidoreductase, 3-hydroxypropionaldehyde reductase, ADH3, dehydrogenase, 1,3-propanediol, DhaT, lr_0030, lr_1734, NADH-dependent 1,3-PD dehydrogenase, NADH-dependent 1,3-propanediol oxidoreductase, NADH-linked 1,3-propanediol oxidoreductase, PDOR, YqhD
ECTree
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Cofactor
Cofactor on EC 1.1.1.202 - 1,3-propanediol dehydrogenase
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NAD+
the enzyme contains a cofactor motif, the conserved sequence G-GG-S-X-X-D. The binding site for cofactor NAD(H) is located in the deep hydrophilic pocket between the PDOR two domains
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NADH
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overexpression of PDOR leads to enhanced NADH and production ratio of NADH/NAD+ exceeds after the inducement of isopropyl-beta-D-thiogalactoside for the constructed strain
NADH
the electrostatic energy is the major force discriminating NADH from NADPH. Residue Asp41 is the key residue responsible for the coenzyme specificity
NADH
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the enzyme prefers NADH to NAD+ as cofactor. 0.5 mM NADH is chosen as optimum concentration
additional information
PDOR requires NAD(H) as a cofactor, but the highly conserved NAD(H) binding fingerprint pattern G-X-G-X-X-G is not present in the amino acid sequence
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